CD81_MOUSE
ID CD81_MOUSE Reviewed; 236 AA.
AC P35762; Q91V78;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=CD81 antigen;
DE AltName: Full=26 kDa cell surface protein TAPA-1;
DE AltName: Full=Target of the antiproliferative antibody 1 {ECO:0000303|PubMed:11046035};
DE AltName: CD_antigen=CD81;
GN Name=Cd81 {ECO:0000303|PubMed:11046035, ECO:0000312|MGI:MGI:1096398};
GN Synonyms=Tapa1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1650385;
RA Andria M.L., Hsieh C.L., Oren R., Francke U., Levy S.;
RT "Genomic organization and chromosomal localization of the TAPA-1 gene.";
RL J. Immunol. 147:1030-1036(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=10915772; DOI=10.1093/hmg/9.12.1829;
RA Paulsen M., El-Maarri O., Engemann S., Stroedicke M., Franck O., Davies K.,
RA Reinhardt R., Reik W., Walter J.;
RT "Sequence conservation and variability of imprinting in the Beckwith-
RT Wiedemann syndrome gene cluster in human and mouse.";
RL Hum. Mol. Genet. 9:1829-1841(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-236.
RC TISSUE=Heart;
RA Duff K., Parsons J.;
RL Submitted (APR-1991) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 125-144; 149-171 AND 194-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11046035; DOI=10.4049/jimmunol.165.9.5054;
RA Deng J., Yeung V.P., Tsitoura D., DeKruyff R.H., Umetsu D.T., Levy S.;
RT "Allergen-induced airway hyperreactivity is diminished in CD81-deficient
RT mice.";
RL J. Immunol. 165:5054-5061(2000).
RN [10]
RP INTERACTION WITH IGSF8.
RX PubMed=11673522; DOI=10.4049/jimmunol.167.9.5115;
RA Clark K.L., Zeng Z., Langford A.L., Bowen S.M., Todd S.C.;
RT "PGRL is a major CD81-associated protein on lymphocytes and distinguishes a
RT new family of cell surface proteins.";
RL J. Immunol. 167:5115-5121(2001).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12796480; DOI=10.1083/jcb.200212031;
RA Takeda Y., Tachibana I., Miyado K., Kobayashi M., Miyazaki T.,
RA Funakoshi T., Kimura H., Yamane H., Saito Y., Goto H., Yoneda T.,
RA Yoshida M., Kumagai T., Osaki T., Hayashi S., Kawase I., Mekada E.;
RT "Tetraspanins CD9 and CD81 function to prevent the fusion of mononuclear
RT phagocytes.";
RL J. Cell Biol. 161:945-956(2003).
RN [12]
RP DISRUPTION PHENOTYPE (MICROBIAL INFECTION), FUNCTION (MICROBIAL INFECTION),
RP AND TISSUE SPECIFICITY.
RX PubMed=12483205; DOI=10.1038/nm808;
RA Silvie O., Rubinstein E., Franetich J.F., Prenant M., Belnoue E., Renia L.,
RA Hannoun L., Eling W., Levy S., Boucheix C., Mazier D.;
RT "Hepatocyte CD81 is required for Plasmodium falciparum and Plasmodium
RT yoelii sporozoite infectivity.";
RL Nat. Med. 9:93-96(2003).
RN [13]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=16380109; DOI=10.1016/j.ydbio.2005.11.031;
RA Rubinstein E., Ziyyat A., Prenant M., Wrobel E., Wolf J.-P., Levy S.,
RA Le Naour F., Boucheix C.;
RT "Reduced fertility of female mice lacking CD81.";
RL Dev. Biol. 290:351-358(2006).
RN [14]
RP INTERACTION WITH IFITM2 AND IFITM3.
RX PubMed=16395393; DOI=10.1038/sj.gene.6364278;
RA Smith R.A., Young J., Weis J.J., Weis J.H.;
RT "Expression of the mouse fragilis gene products in immune cells and
RT association with receptor signaling complexes.";
RL Genes Immun. 7:113-121(2006).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18662991; DOI=10.1074/jbc.m801902200;
RA Takeda Y., He P., Tachibana I., Zhou B., Miyado K., Kaneko H., Suzuki M.,
RA Minami S., Iwasaki T., Goya S., Kijima T., Kumagai T., Yoshida M.,
RA Osaki T., Komori T., Mekada E., Kawase I.;
RT "Double deficiency of tetraspanins CD9 and CD81 alters cell motility and
RT protease production of macrophages and causes chronic obstructive pulmonary
RT disease-like phenotype in mice.";
RL J. Biol. Chem. 283:26089-26097(2008).
RN [16]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND FUNCTION IN ACROSOME
RP REACTION.
RX PubMed=17290409; DOI=10.1002/mrd.20709;
RA Tanigawa M., Miyamoto K., Kobayashi S., Sato M., Akutsu H., Okabe M.,
RA Mekada E., Sakakibara K., Miyado M., Umezawa A., Miyado K.;
RT "Possible involvement of CD81 in acrosome reaction of sperm in mice.";
RL Mol. Reprod. Dev. 75:150-155(2008).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [18]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23213457; DOI=10.1242/bio.20121420;
RA Ohnami N., Nakamura A., Miyado M., Sato M., Kawano N., Yoshida K.,
RA Harada Y., Takezawa Y., Kanai S., Ono C., Takahashi Y., Kimura K.,
RA Shida T., Miyado K., Umezawa A.;
RT "CD81 and CD9 work independently as extracellular components upon fusion of
RT sperm and oocyte.";
RL Biol. Open 1:640-647(2012).
RN [19]
RP INTERACTION WITH GPC3 AND HHEX.
RX PubMed=23665349; DOI=10.1016/j.ajpath.2013.03.013;
RA Bhave V.S., Mars W., Donthamsetty S., Zhang X., Tan L., Luo J., Bowen W.C.,
RA Michalopoulos G.K.;
RT "Regulation of liver growth by glypican 3, CD81, hedgehog, and Hhex.";
RL Am. J. Pathol. 183:153-159(2013).
RN [20]
RP FUNCTION.
RX PubMed=23499492; DOI=10.1016/j.immuni.2012.11.019;
RA Mattila P.K., Feest C., Depoil D., Treanor B., Montaner B., Otipoby K.L.,
RA Carter R., Justement L.B., Bruckbauer A., Batista F.D.;
RT "The actin and tetraspanin networks organize receptor nanoclusters to
RT regulate B cell receptor-mediated signaling.";
RL Immunity 38:461-474(2013).
RN [21]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION BY MYOTOXIC
RP AGENTS, INTERACTION WITH PTGFRN, INTERACTION WITH CD9, AND INTERACTION WITH
RP IGSF8.
RX PubMed=23575678; DOI=10.1038/ncomms2675;
RA Charrin S., Latil M., Soave S., Polesskaya A., Chretien F., Boucheix C.,
RA Rubinstein E.;
RT "Normal muscle regeneration requires tight control of muscle cell fusion by
RT tetraspanins CD9 and CD81.";
RL Nat. Commun. 4:1674-1674(2013).
RN [22] {ECO:0007744|PDB:3X0F}
RP X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF 113-202, AND DISULFIDE BONDS.
RX PubMed=26116703; DOI=10.1096/fj.15-272880;
RA Yang W., Zhang M., Chi X., Liu X., Qin B., Cui S.;
RT "An intramolecular bond at cluster of differentiation 81 ectodomain is
RT important for hepatitis C virus entry.";
RL FASEB J. 29:4214-4226(2015).
CC -!- FUNCTION: Structural component of specialized membrane microdomains
CC known as tetraspanin-enriched microdomains (TERMs), which act as
CC platforms for receptor clustering and signaling. Essential for
CC trafficking and compartmentalization of CD19 receptor on the cell
CC surface of activated B cells (PubMed:23499492). Upon initial encounter
CC with a microbial pathogen, enables the assembly of CD19-CR2 and B cell
CC receptor complexes at signaling TERMs, lowering the threshold dose of
CC antigen required to trigger B cell clonal expansion and humoral immune
CC response (By similarity). In T cells, associates with CD4 or CD8
CC coreceptors and defines the maturation state of antigen-induced
CC synapses with B cells (By similarity). Facilitates localization of CD3
CC in these immune synapses, required for costimulation and sustained
CC activation of T cells, preferentially triggering T helper type 2 immune
CC response (PubMed:11046035). Can act both as positive and negative
CC regulator of homotypic or heterotypic cell-cell fusion processes. In
CC myoblasts, associates with another tetraspanin CD9 in complex with
CC PTGFRN and inhibits myotube fusion during muscle regeneration
CC (PubMed:23575678). In macrophages, associates with CD9 and beta-1 and
CC beta-2 integrins, and prevents macrophage fusion into multinucleated
CC giant cells specialized in ingesting complement-opsonized large
CC particles. Also prevents the fusion between mononuclear cell
CC progenitors into osteoclasts in charge of bone resorption. Positively
CC regulates sperm-egg fusion and may be involved in the acrosome reaction
CC (PubMed:16380109, PubMed:17290409). Regulates protein trafficking in
CC intracellular compartments. In T cells, associates with dNTPase SAMHD1
CC and defines its subcellular location, enabling its degradation by the
CC proteasome and thereby controlling intracellular dNTP levels (By
CC similarity). Also regulates integrin-dependent migration of
CC macrophages, particularly relevant for inflammatory response in the
CC lung (PubMed:18662991). {ECO:0000250|UniProtKB:P60033,
CC ECO:0000269|PubMed:11046035, ECO:0000269|PubMed:16380109,
CC ECO:0000269|PubMed:17290409, ECO:0000269|PubMed:18662991,
CC ECO:0000269|PubMed:23499492, ECO:0000269|PubMed:23575678}.
CC -!- FUNCTION: (Microbial infection) Specifically required for Plasmodium
CC yoelii infectivity of hepatocytes, controlling sporozoite entry in
CC hepatocytes via the parasitophorous vacuole and subsequent parasite
CC differentiation to exoerythrocytic forms.
CC {ECO:0000269|PubMed:12483205}.
CC -!- SUBUNIT: Homodimer (By similarity). Part of a complex composed of CD19,
CC CR2/CD21, CD81 and IFITM1/CD225 in the membrane of mature B cells.
CC Interacts (via the second extracellular domain) with CD19; this
CC interaction is initiated early during biosynthesis in the ER and
CC enables trafficking of only properly folded CD19 (By similarity). Part
CC of a complex that includes MHC class II/HLA-DR molecules and IFITM1.
CC Interacts with IFITM1 (By similarity). Interacts with IFITM2 and IFITM3
CC (PubMed:16395393). Part of integrin-tetraspanin complex composed of
CC CD9, CD81, beta-1 and beta-2 integrins in the membrane of
CC monocyte/macrophages (By similarity). Interacts (via the second
CC extracellular domain) with integrin ITGAV:ITGB3 (By similarity).
CC Interacts with CD247/CD3 zeta, ICAM1 and CD9 at the immune synapse on T
CC cell membrane (By similarity). Part of a GPCR-tetraspanin complex
CC consisting at least of ADGRG1, CD81, possibly CD9, and GNA11 in which
CC CD81 enhances the association of ADGRG1 with GNA11 (By similarity).
CC Part of a complex composed of CD9, CD81, PTGFRN and IGSF8
CC (PubMed:23575678). Interacts directly with IGSF8 (PubMed:11673522).
CC Interacts with CD53 and SCIMP (By similarity). Interacts with SAMHD1
CC (via its C-terminus) (By similarity). Interacts with glypican GPC3 and
CC with the transcriptional repressor HHEX; binding to GPC3 decreases the
CC availability of free CD81 for binding to HHEX, resulting in nuclear
CC translocation of HHEX and transcriptional repression (PubMed:23665349).
CC Interacts with CLDN1 (By similarity). Interacts with CLDN6 and CLDN9
CC (By similarity). {ECO:0000250|UniProtKB:P60033,
CC ECO:0000269|PubMed:11673522, ECO:0000269|PubMed:16395393,
CC ECO:0000269|PubMed:23575678, ECO:0000269|PubMed:23665349}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23213457};
CC Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:P60033}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Associates with CLDN1 and the CLDN1-CD81 complex
CC localizes to the basolateral cell membrane.
CC {ECO:0000250|UniProtKB:P60033}.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes (at protein level)
CC (PubMed:16380109, PubMed:17290409, PubMed:23213457). Highly expressed
CC in granulosa cells (PubMed:16380109). Expressed in skeletal muscle
CC mainly in endothelial cells of endomysial capillaries, in satellite
CC cells and myoblasts (at protein level) (PubMed:23575678). Expressed in
CC hepatocytes (at protein level) (PubMed:12483205).
CC {ECO:0000269|PubMed:12483205, ECO:0000269|PubMed:16380109,
CC ECO:0000269|PubMed:17290409, ECO:0000269|PubMed:23213457,
CC ECO:0000269|PubMed:23575678}.
CC -!- INDUCTION: Up-regulated in response to notexin-induced acute myoinjury.
CC {ECO:0000269|PubMed:23575678}.
CC -!- DOMAIN: Binds cholesterol in a cavity lined by the transmembrane spans.
CC {ECO:0000250|UniProtKB:P60033}.
CC -!- PTM: Not glycosylated. {ECO:0000305}.
CC -!- PTM: Likely constitutively palmitoylated at low levels. Protein
CC palmitoylation is up-regulated upon coligation of BCR and CD9-C2R-CD81
CC complexes in lipid rafts. {ECO:0000250|UniProtKB:P60033}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice exhibit reduced female fertitily
CC and impaired egg-sperm fusion (PubMed:16380109, PubMed:17290409). In
CC response to notexin-induced acute myoinjury, mutant mice display
CC abnormal muscle regeneration characterized by typical giant distrophic
CC myofibres (PubMed:23575678). Mutant mice show reduced allergen-induced
CC lung inflammation, eosinophilia and mucin production (PubMed:11046035).
CC These mice spontaneously develop multinucleated giant cells (MGCs) and
CC show enhanced osteoclastogenesis when compared to wild-type littermates
CC (PubMed:12796480). CD81 and CD9 double knockout mice develop pulmonary
CC emphysema, reminiscent of chronic obstructive pulmonary disease in
CC human (PubMed:18662991). {ECO:0000269|PubMed:11046035,
CC ECO:0000269|PubMed:12796480, ECO:0000269|PubMed:16380109,
CC ECO:0000269|PubMed:17290409, ECO:0000269|PubMed:18662991,
CC ECO:0000269|PubMed:23575678}.
CC -!- DISRUPTION PHENOTYPE: (Microbial infection) Mutant mice are refractory
CC to Plasmodium yoelii sporozoite infection.
CC {ECO:0000269|PubMed:12483205}.
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR EMBL; S45012; AAB19417.1; -; Genomic_DNA.
DR EMBL; S44957; AAB19417.1; JOINED; Genomic_DNA.
DR EMBL; S44966; AAB19417.1; JOINED; Genomic_DNA.
DR EMBL; S45001; AAB19417.1; JOINED; Genomic_DNA.
DR EMBL; S45008; AAB19417.1; JOINED; Genomic_DNA.
DR EMBL; S45010; AAB19417.1; JOINED; Genomic_DNA.
DR EMBL; AJ251835; CAB94774.1; -; Genomic_DNA.
DR EMBL; AK166521; BAE38825.1; -; mRNA.
DR EMBL; AK170741; BAE41994.1; -; mRNA.
DR EMBL; AC015800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466531; EDL18195.1; -; Genomic_DNA.
DR EMBL; BC011433; AAH11433.1; -; mRNA.
DR EMBL; X59047; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS22038.1; -.
DR PIR; A46472; A46472.
DR RefSeq; NP_598416.1; NM_133655.2.
DR PDB; 3X0F; X-ray; 1.47 A; A/B=113-202.
DR PDBsum; 3X0F; -.
DR AlphaFoldDB; P35762; -.
DR SMR; P35762; -.
DR BioGRID; 198613; 20.
DR IntAct; P35762; 1.
DR STRING; 10090.ENSMUSP00000043768; -.
DR iPTMnet; P35762; -.
DR PhosphoSitePlus; P35762; -.
DR SwissPalm; P35762; -.
DR EPD; P35762; -.
DR jPOST; P35762; -.
DR PaxDb; P35762; -.
DR PeptideAtlas; P35762; -.
DR PRIDE; P35762; -.
DR ProteomicsDB; 265630; -.
DR Antibodypedia; 1570; 1293 antibodies from 46 providers.
DR DNASU; 12520; -.
DR Ensembl; ENSMUST00000037941; ENSMUSP00000043768; ENSMUSG00000037706.
DR GeneID; 12520; -.
DR KEGG; mmu:12520; -.
DR UCSC; uc009kou.2; mouse.
DR CTD; 975; -.
DR MGI; MGI:1096398; Cd81.
DR VEuPathDB; HostDB:ENSMUSG00000037706; -.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000158805; -.
DR HOGENOM; CLU_055524_10_0_1; -.
DR InParanoid; P35762; -.
DR OMA; HETLSCC; -.
DR OrthoDB; 1205716at2759; -.
DR PhylomeDB; P35762; -.
DR TreeFam; TF352895; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 12520; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Cd81; mouse.
DR PRO; PR:P35762; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P35762; protein.
DR Bgee; ENSMUSG00000037706; Expressed in aortic valve and 273 other tissues.
DR ExpressionAtlas; P35762; baseline and differential.
DR Genevisible; P35762; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0001772; C:immunological synapse; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0097197; C:tetraspanin-enriched microdomain; ISS:UniProtKB.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0015485; F:cholesterol binding; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0042289; F:MHC class II protein binding; ISO:MGI.
DR GO; GO:1990459; F:transferrin receptor binding; ISO:MGI.
DR GO; GO:0001618; F:virus receptor activity; ISO:MGI.
DR GO; GO:0035783; P:CD4-positive, alpha-beta T cell costimulation; ISS:UniProtKB.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IDA:UniProtKB.
DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; ISS:UniProtKB.
DR GO; GO:0001771; P:immunological synapse formation; ISS:UniProtKB.
DR GO; GO:0034238; P:macrophage fusion; IMP:UniProtKB.
DR GO; GO:0014905; P:myoblast fusion involved in skeletal muscle regeneration; IMP:UniProtKB.
DR GO; GO:0072675; P:osteoclast fusion; IMP:UniProtKB.
DR GO; GO:0043128; P:positive regulation of 1-phosphatidylinositol 4-kinase activity; ISS:UniProtKB.
DR GO; GO:1905676; P:positive regulation of adaptive immune memory response; ISO:MGI.
DR GO; GO:0050871; P:positive regulation of B cell activation; IMP:UniProtKB.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; ISO:MGI.
DR GO; GO:0050861; P:positive regulation of B cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; ISS:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; TAS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0002863; P:positive regulation of inflammatory response to antigenic stimulus; IMP:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:1904352; P:positive regulation of protein catabolic process in the vacuole; ISO:MGI.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:1903911; P:positive regulation of receptor clustering; IMP:UniProtKB.
DR GO; GO:2001190; P:positive regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IMP:UniProtKB.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:2000553; P:positive regulation of T-helper 2 cell cytokine production; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR GO; GO:0061462; P:protein localization to lysosome; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
DR GO; GO:2000145; P:regulation of cell motility; IGI:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:MGI.
DR GO; GO:1905521; P:regulation of macrophage migration; IDA:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
DR Gene3D; 1.10.1450.10; -; 1.
DR InterPro; IPR018499; Tetraspanin/Peripherin.
DR InterPro; IPR000301; Tetraspanin_animals.
DR InterPro; IPR018503; Tetraspanin_CS.
DR InterPro; IPR008952; Tetraspanin_EC2_sf.
DR PANTHER; PTHR19282; PTHR19282; 1.
DR Pfam; PF00335; Tetraspanin; 1.
DR PIRSF; PIRSF002419; Tetraspanin; 1.
DR SUPFAM; SSF48652; SSF48652; 1.
DR PROSITE; PS00421; TM4_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Immunity; Lipid-binding; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..236
FT /note="CD81 antigen"
FT /id="PRO_0000219222"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P60033"
FT TOPO_DOM 34..63
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P60033"
FT TOPO_DOM 85..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 90..112
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P60033"
FT TOPO_DOM 113..201
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 202..224
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P60033"
FT TOPO_DOM 225..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 219
FT /ligand="cholesterol"
FT /ligand_id="ChEBI:CHEBI:16113"
FT /evidence="ECO:0000250|UniProtKB:P60033"
FT SITE 116
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P60033"
FT SITE 144
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P60033"
FT SITE 148
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P60033"
FT DISULFID 156..190
FT /evidence="ECO:0000269|PubMed:26116703,
FT ECO:0007744|PDB:3X0F"
FT DISULFID 157..175
FT /evidence="ECO:0000269|PubMed:26116703,
FT ECO:0007744|PDB:3X0F"
FT CONFLICT 173
FT /note="S -> T (in Ref. 1; AAB19417)"
FT /evidence="ECO:0000305"
FT HELIX 116..136
FT /evidence="ECO:0007829|PDB:3X0F"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:3X0F"
FT HELIX 161..170
FT /evidence="ECO:0007829|PDB:3X0F"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:3X0F"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:3X0F"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:3X0F"
SQ SEQUENCE 236 AA; 25815 MW; 7BDCB792E7F9FA4E CRC64;
MGVEGCTKCI KYLLFVFNFV FWLAGGVILG VALWLRHDPQ TTSLLYLELG NKPAPNTFYV
GIYILIAVGA VMMFVGFLGC YGAIQESQCL LGTFFTCLVI LFACEVAAGI WGFVNKDQIA
KDVKQFYDQA LQQAVMDDDA NNAKAVVKTF HETLNCCGSN ALTTLTTTIL RNSLCPSGGN
ILTPLLQQDC HQKIDELFSG KLYLIGIAAI VVAVIMIFEM ILSMVLCCGI RNSSVY
